The stabilization of in vivo assembled collagen fibrils by proteoglycans/glycosaminoglycans.
The effects of proteoglycans/glycosaminoglycans on the thermal stability of in vivo assembled collagen fibrils have been examined. The shrinkage temperature of tendon collagen was found to be linearly dependent on the concentration of chondroitin sulphate in the surrounding fluid. Enzymic pretreatment of articular cartilage, to reduce its glycosaminoglycan content, resulted in decreased stability of the collagen present. The stability of the collagen in hyaluronidase-treated cartilage was found to be higher when measured in a solution of chondroitin sulphate (30 g/dl) than in buffer alone. The results of this study demonstrate that the proteoglycans stabilize collagen fibrils in tissues such as articular cartilage.
D000818:Animals; D002358:Cartilage, Articular / Q000033:anatomy & histology* / Q000187:drug effects; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D002809:Chondroitin Sulfates / Q000494:pharmacology*; D003094:Collagen / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006358:Hot Temperature; D006821:Hyaluronoglucosaminidase / Q000378:metabolism; D011489:Protein Denaturation; D014357:Trypsin / Q000378:metabolism
D006025:Glycosaminoglycans; D002807:Chondroitin; D002809:Chondroitin Sulfates; D003094:Collagen; D006821:Hyaluronoglucosaminidase; D014357:Trypsin